simultaneous expression of carboxylesterase B1 and organophosphorus hydrolase EC 3.1.8.1 in Escherichia coli and use of vacuum dried cells for decontamination of vegetables sprayed with organophosphate pesticides. Activities of enzymes remain stable in dried cells for at least 5 months. Crude enzymes in 50 mM citrate-phosphate buffer are able to degrade 97% of the organophosphates sprayed on cabbage to virtually nontoxic products
use of fluorescence-activated cell sorting and methylumbelliferyl acetate substrate for identification of carboxylesterases and high-throughput screening
the enzyme with substrate (S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone and inhibitor bis(p-nitrophenyl) phosphate are useful in a system to measure in plasma-free fraction for a plasma-labile compound
the enzyme with substrate (S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone and inhibitor bis(p-nitrophenyl) phosphate are useful in a system to measure in plasma-free fraction for a plasma-labile compound
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
use of enzyme as a more sensitive biomarker for exposure to organophosphate than acetylcholinesterase. Enzyme is not suitable as a biomarker for pyrethroid exposure
SexiCXE10 acts as a general odorant-degrading enzyme, showing the potential to be a target for developing behavioral antagonists and pesticides against Spodoptera exigua
use of enzyme to remove permethrin- and bifenthrin-associated toxicity to Ceriodaphna dubia and Hyalella axteca in a variety of matrices, including laboratory water, river water, river interstitial water, municipal effluent and seawater
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
the catalytic efficiencies (kcat/Km) of Fluazifop-P-butyl carboxylesterase (FpbH) for different AOPP herbicides are higher than those of Cyhalofop-butyl esterase (ChbH) from Pseudomonas azotoformans and Fenoxaprop-ethyl hydrolase (FeH) from Rhodococcus sp.. FpbH differs from previously reported AOPP herbicide carboxylesterases and might be a good candidate enzyme for biodegradation, especially when diclofop-methyl and/or haloxyfop-P-methyl are the dominant pollutants
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
enzyme can activate prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin to give 7-ethyl-10-hydroxycampothecin, i.e. SN-38, a topoisomerase inhibitor used in cancer therapy
human small intestine and liver show extensive hydrolase activity attributed to carboxylesterase, which is different from that in species normally used as experimental animals
intestinal carboxyesterase is the enzyme that activates doxazolidine carbamate prodrug Pentyl PABC-Doxaz. MCF-7 cells or U-373MG cells overexpressing the enzyme show dramatically reduced IC50 values for Pentyl PABC-Doxaz
isolation of mutant enzyme hCE1m6, which is 70fold more efficient in cleavage of the antitumor prodrug irinotecan-7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin, i.e. CPT-11, than wild-type. Adenoviral-mediated delivery of mutant enzyme with human tumor cells results in up to 670fold reduction in the IC50 value for CPT-11
isolation of mutant enzyme hCE1m6, which is 70fold more efficient in cleavage of the antitumor prodrug irinotecan-7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin, i.e. CPT-11, than wild-type. Adenoviral-mediated delivery of mutant enzyme with human tumor cells results in up to 670fold reduction in the IC50 value for CPT-11
since the enzyme may be useful as a treatment for cocaine overdose, and may afford protection against chemical weapons like Sarin, Soman and VX gas, hCE1 could serve as both a drug and a drug target
enzyme overexpression in colorectal cancer and cancer cell death stemming from its inhibition is an indication of its possible role in cancer progression and a target for chemopreventive agents
methyl hydrogen (1S,2R)-cyclohex-4-ene-1,2-dicarboxylate is an important educt for the synthesis of diverse biologically relevant products such as carbacyclin, prostaglandin synthon, brefeldin, anticapsin and others
the enzyme is useful for the synthesis of 1-monocaprin, a widely used functional emulsifier in the food, cosmetic, and pharmaceutical industries and is recognized as a GRAS food additive
synthesis of poly(delta-valerolactone) in organic solvents. The synthesized poly(delta-valerolactone) is of low molecular weight and narrow molecular weight distribution, and is expected to be widely used as the soft block of thermoplastic elastomers, or carriers for controlled drug delivery and release
the enzyme shows chiral resolution activity for (S)-ibuprofen, indicating that the enzyme can be used for the production of commercially important chiral drugs
synthesis of (S)-alpha-arylpropionates (profens). The reaction proceeds via enantioselective hydrolysis of the malonic acid ester to the monoester. Cleavage of the carboxyl group at the active site of the enzyme leads to the formation of the prochiral intermediate, which is then protonated to give the enantioenriched monoacid. Engineering of the active site gives rise to a variant with good stereoselectivity. As the esterase-catalyzed domino reaction does not need external cofactors and allows a theoretical yield of 100%
enzyme shows high enantioselectivity in the kinetic resolution of 2-carboxyethyl-3-cyano-5-methylhexanoic acid ethyl ester, which produce a valuable chiral intermediate-(3S)-2-carboxyethyl-3-cyano-5-methylhexanoic acid for the drug Pregabalin
synthesis of (S)-alpha-arylpropionates (profens). The reaction proceeds via enantioselective hydrolysis of the malonic acid ester to the monoester. Cleavage of the carboxyl group at the active site of the enzyme leads to the formation of the prochiral intermediate, which is then protonated to give the enantioenriched monoacid. Engineering of the active site gives rise to a variant with good stereoselectivity. As the esterase-catalyzed domino reaction does not need external cofactors and allows a theoretical yield of 100%
the enzyme shows chiral resolution activity for (S)-ibuprofen, indicating that the enzyme can be used for the production of commercially important chiral drugs
enzyme shows high enantioselectivity in the kinetic resolution of 2-carboxyethyl-3-cyano-5-methylhexanoic acid ethyl ester, which produce a valuable chiral intermediate-(3S)-2-carboxyethyl-3-cyano-5-methylhexanoic acid for the drug Pregabalin